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HipBA毒素-抗毒素系统采用了一种不同寻常的三组分调节机制。

The HipBA toxin-antitoxin system adopts an unusual three-com-ponent regulatory mechanism.

作者信息

Koo Ji Sung, Kang Sung-Min, Jung Won-Min, Kim Do-Hee, Lee Bong-Jin

机构信息

Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul 08826, Republic of Korea.

College of Pharmacy, Duksung Women's University, Seoul 01369, Republic of Korea.

出版信息

IUCrJ. 2022 Jul 29;9(Pt 5):625-631. doi: 10.1107/S205225252200687X. eCollection 2022 Sep 1.

DOI:10.1107/S205225252200687X
PMID:36071804
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9438503/
Abstract

Type II toxin-antitoxin (TA) systems encode two proteins: a toxin that inhibits cell growth and an antitoxin that neutralizes the toxin by direct inter-molecular protein-protein inter-actions. The bacterial HipBA TA system is implicated in persister formation. The HipBA TA system consists of a HipB antitoxin and a HipA toxin, the latter of which is split into two fragments, and here we investigate this novel three-com-ponent regulatory HipBA system. Structural and functional analysis revealed that HipA corresponds to the N-ter-minal part of HipA from other bacteria and toxic HipA is inactivated by HipA, not HipB. This study will be helpful in understanding the detailed regulatory mechanism of the HipBA system, as well as why it is constructed as a three-com-ponent system.

摘要

II型毒素-抗毒素(TA)系统编码两种蛋白质:一种抑制细胞生长的毒素和一种通过直接分子间蛋白质-蛋白质相互作用中和毒素的抗毒素。细菌HipBA TA系统与持留菌的形成有关。HipBA TA系统由HipB抗毒素和HipA毒素组成,后者被分成两个片段,在此我们研究这种新型的三组分调节HipBA系统。结构和功能分析表明,HipA对应于其他细菌中HipA的N末端部分,有毒的HipA被HipA而非HipB失活。这项研究将有助于理解HipBA系统的详细调节机制,以及它为何被构建为三组分系统。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/24d4/9438503/1c6f8d326427/m-09-00625-fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/24d4/9438503/c9beb12733a8/m-09-00625-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/24d4/9438503/7a26d9808edf/m-09-00625-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/24d4/9438503/5595336b7b77/m-09-00625-fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/24d4/9438503/1c6f8d326427/m-09-00625-fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/24d4/9438503/c9beb12733a8/m-09-00625-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/24d4/9438503/7a26d9808edf/m-09-00625-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/24d4/9438503/5595336b7b77/m-09-00625-fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/24d4/9438503/1c6f8d326427/m-09-00625-fig4.jpg

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本文引用的文献

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Serine/Threonine Protein Kinases from Bacteria, Archaea and Eukarya Share a Common Evolutionary Origin Deeply Rooted in the Tree of Life.来自细菌、古菌和真核生物的丝氨酸/苏氨酸蛋白激酶有着共同的进化起源,深深植根于生命之树。
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可消耗元件的重要性:质粒和染色体中的毒素-抗毒素基因
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